The Role of the Src Homology 3-Src Homology 2 Interface in the Regulation of Src Kinases

Journal of Biological Chemistry

Volumn 276, Issue 20, 2001, Pages 17199-17205

  Arold, Stefan T ^a   Ulmer, Tobias S ^b   Mulhern, Terrence D ^d   Werner, Jörn M ^b   Ladbury, John E ^c   Campbell, Iain D ^b   Noble, Martin E M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY COLLEGE LONDON   (United Kingdom)

^d UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETRY; CRYSTALLOGRAPHY; ENZYME KINETICS; ISOTHERMS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHYSIOLOGY;

HOMOLOGY;

BIOCHEMISTRY;

FOCAL ADHESION KINASE; GENE PRODUCT; PHOSPHOTYROSINE; POLYPROLINE; PROLINE DERIVATIVE; PROTEIN; PROTEIN FYNSH32; PROTEIN KINASE FYN; PROTEIN KINASE LCK; PROTEIN KINASE P60; PROTEIN LCKSH32; UNCLASSIFIED DRUG; FYK KINASE; PEPTIDE; PROTEIN TYROSINE KINASE; RECOMBINANT PROTEIN;

ANTIGEN RECOGNITION; ARTICLE; BINDING AFFINITY; BINDING SITE; CALORIMETRY; CHEMICAL INTERACTION; CRYSTALLOGRAPHY; DISSOCIATION; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME REGULATION; ENZYME REPRESSION; ENZYME SPECIFICITY; FYNSH32 GENE; ISOTHERMAL TITRATION CALORIMETRY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; REGULATOR GENE; REGULATORY MECHANISM; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; SRC HOMOLOGY 2 DOMAIN; SRC HOMOLOGY 3 DOMAIN; SRC HOMOLOGY DOMAIN; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; HUMAN; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; CALORIMETRY; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PHOSPHOTYROSINE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN-TYROSINE KINASES; RECOMBINANT PROTEINS; SRC HOMOLOGY DOMAINS; SRC-FAMILY KINASES;

EID: 0035907348     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M011185200     Document Type: Article

References (39)

1. Williams, J. C., Weijland, A., Gonfloni, S., Thompson, A., Courtneidge, S. A., Superti-Furga, G., and Wierenga, R. K. (1997) J. Mol. Biol. 274, 757-775
2. Xu, W., Harrison, S. C., and Eck, M. J. (1997) Nature 385, 595-602
3. Sicheri, F., Moarefi, I., and Kuriyan, J. (1997) Nature 385, 602-609
4. Moarefi, I., LaFevre-Bernt, M., Sicheri, F., Huse, M., Lee, C. H., Kuriyan, J., and Miller, W. T. (1997) Nature 385, 650-653
5. Cobb, B. S., Schaller, M. D., Leu, T. H., and Parsons, J. T. (1994) Mol. Cell. Biol. 14, 147-155
6. Thomas, J. W., Ellis, B., Boerner, R. J., Knight, W. B., White, G. C., II, and Schaller, M. D. (1998) J. Biol. Chem. 273, 577-583
7. Taylor, S. J., and Shalloway, D. (1994) Nature 368, 867-871
8. Xing, Z., Chen, H. C., Nowlen, J. K., Taylor, S. J., Shalloway, D., and Guan, J. L. (1994) Mol. Biol. Cell 5, 413-421
9. Richard, S., Yu, D., Blumer, K. J., Hausladen, D., Olszowy, M. W., Connelly, P. A., and Shaw, A. S. (1995) Mol. Cell. Biol. 15, 186-197
10. Nakamoto, T., Sakai, R., Ozawa, K., Yazaki, Y., and Hirai, H. (1996) J. Biol. Chem. 271, 8959-8965
11. Alexandropoulos, K., and Baltimore, D. (1996) Genes Dev. 10, 1341-13455
12. Flynn, D. C., Leu, T. H., Reynolds, A. B., and Parsons, J. T. (1993) Mol. Cell. Biol. 13, 7892-7900
13. Gonfloni, S., Weijland, A., Kretzschmar, J., and Superti-Furga, G. (2000) Nat. Struct. Biol. 7, 281-286
14. Porter, M., Schindler, T., Kuriyan, J., and Miller, W. T. (2000) J. Biol. Chem. 275, 2721-2726
15. Ilic, D., Damsky, C. H., and Yarnamoto, T. (1997) J. Cell Sci. 110, 401-407
16. Jones, R. J., Brunton, V. G., and Frame, M. C. (2000) Eur. J. Cancer 36, 1595-1606
17. Boyd, J., Soffe, N., John, B., Plant, D., and Hurd, R. (1992) J. Magn. Reson. 98, 660-664
18. Grzesiek, S., and Bax, A. (1993) J. Am. Chem. Soc. 115, 12593-12594
19. Jahnke, W., Baur, M., Gemmecker, G., and Kessler, H. (1995) J. Magn. Reson. Series B 106, 86-88
20. Salzmann, M., Wider, G., Pervushin, K., Senn, H., and Wuthrich, K. (1999) J. Am. Chem. Soc. 121, 844-848
21. Morton, C. J., Pugh, D. J. R., Brown, E. L. J., Kahmann, J. D., Renzoni, D. A. C., and Campbell, I. D. (1996) Structure 4, 705-714
22. Mulhern, T. D., Shaw, G. L., Morton, C. J., Day, A. J., and Campbell, I. D. (1997) Structure 5, 1313-1323
23. Bartels, C., Xia, T. H., Billeter, M., Guntert, P., and Wuthrich, K. (1995) J. Biomol. NMR 6, 1-10
24. Kay, L. E., Torchia, D. A., and Bax, A. (1989) Biochemistry 28, 8972-8979
25. Farrow, N. A., Zhang, O. W., Formankay, J. D., and Kay, L. E. (1994) J. Biomol. NMR 4, 727-734
26. Boyd, J., Hommel, U., and Campbell, I. D. (1990) Chem. Phys. Lett. 175, 477-482
27. Kay, L. E., Nicholson, L. K., Delaglio, F., Bax, A., and Torchia, D. A. (1992) J. Magn. Reson. 97, 359-375
28. Palmer, A. G., Rance, M., and Wright, P. E. (1991) J. Am. Chem. Soc. 113, 4371-4380
29. Fushman, D., Xu, R., and Cowburn, D. (1999) Biochemistry 38, 10225-10230
30. Ladbury, J. E., Hensmann, M., Panayotou, G., and Campbell, I. D. (1996) Biochemistry 35, 11062-11069
31. Waksman, G., Shoelson, S. E., Pant, N., Cowburn, D., and Kuriyan, J. (1993) Cell 72, 779-790
32. Maignan, S., Guilloteau, J. P., Fromage, N., Arnoux, B., Becquart, J., and Ducruix, A. (1995) Science 268, 291-293
33. Eck, M. J., Atwell, S. K., Shoelson, S. E., and Harrison, S. C. (1994) Nature 368, 764-769
34. Briggs, S. D., Lerner, E. C., and Smithgall, T. E. (2000) Biochemistry 39, 489-495
35. Huse, M., Eck, M. J., and Harrison, S. C. (1998) J. Biol. Chem. 273, 18729-18733
36. Brown, M. T., and Cooper, J. A. (1996) Biochim. Biophys. Acta 1287, 121-149
37. Shen, Y., and Schaller, M. D. (1999) Mol. Biol. Cell 10, 2507-2518
38. Sasaki, H., Nagura, K., Ishino, M., Tobioka, H., Kotani, K., and Sasaki, T. (1995) J. Biol. Chem. 275, 21206-21219
39. Arold, S., Franken, P., Strub, M. P., Hoh, F., Benichou, S., Benarous, R., and Dumas, C. (1997) Structure 5, 1361-1372